The Extracellular Matrix Receptor Discoidin Domain Receptor 1 Regulates Collagen Transcription by Translocating to the Nucleus
Author(s) -
Manuel Chiusa,
Wen Hu,
HongJun Liao,
Yan Ru Su,
Corina M. Borza,
Mark P. de Caestecker,
Nataliya Skrypnyk,
Agnes B. Fogo,
Vadim Pedchenko,
Xiyue Li,
MingZhi Zhang,
Billy G. Hudson,
Trayambak Basak,
Roberto Vanacore,
Roy Zent,
Ambra Pozzi
Publication year - 2019
Publication title -
journal of the american society of nephrology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.451
H-Index - 279
eISSN - 1533-3450
pISSN - 1046-6673
DOI - 10.1681/asn.2018111160
Subject(s) - ddr1 , discoidin domain , collagen receptor , receptor tyrosine kinase , microbiology and biotechnology , biology , chemistry , receptor , signal transduction , integrin , biochemistry
The discoidin domain receptor 1 (DDR1) is activated by collagens, upregulated in injured and fibrotic kidneys, and contributes to fibrosis by regulating extracellular matrix production, but how DDR1 controls fibrosis is poorly understood. DDR1 is a receptor tyrosine kinase (RTK). RTKs can translocate to the nucleus via a nuclear localization sequence (NLS) present on the receptor itself or a ligand it is bound to. In the nucleus, RTKs regulate gene expression by binding chromatin directly or by interacting with transcription factors.
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